[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-15. STRAIN=K1-23; TRANSPOSON=Tn5306; DOI=10.1074/jbc.270.20.12226; PubMed=7744873 [NCBI, ExPASy, EBI, Israel, Japan] Donkersloot J.A., Thompson J.; "Cloning, expression, sequence analysis, and site-directed mutagenesis of the Tn5306-encoded N(5)-(carboxyethyl)ornithine synthase from Lactococcus lactis K1."; J. Biol. Chem. 270:12226-12234(1995).
[2]	PROTEIN SEQUENCE OF 1-37. STRAIN=K1; PubMed=2498334 [NCBI, ExPASy, EBI, Israel, Japan] Thompson J.; "N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase from Streptococcus lactis. Purification and partial characterization."; J. Biol. Chem. 264:9592-9601(1989).
[3]	PROTEIN SEQUENCE OF 256-263, CHARACTERIZATION, AND MASS SPECTROMETRY. STRAIN=K1; PubMed=10548058 [NCBI, ExPASy, EBI, Israel, Japan] Sackett D.L., Ruvinov S.B., Thompson J.; "N(5)-(L-1-carboxyethyl)-L-ornithine synthase: physical and spectral characterization of the enzyme and its unusual low pKa fluorescent tyrosine residues."; Protein Sci. 8:2121-2129(1999).
[4]	FOLDING STUDIES. STRAIN=K1; DOI=10.1006/abbi.1999.1429; PubMed=10525296 [NCBI, ExPASy, EBI, Israel, Japan] Ruvinov S.B., Thompson J., Sackett D.L., Ginsburg A.; "Tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase: guanidine. HCl-induced unfolding and a low temperature requirement for refolding."; Arch. Biochem. Biophys. 371:115-123(1999).

Comments

CATALYTIC ACTIVITY: N⁵-(L-1-carboxyethyl)-L-ornithine + NADP⁺ + H₂O = L-ornithine + pyruvate + NADPH.
SUBUNIT: Homotetramer.
MASS SPECTROMETRY: Mass=35355; Method=MALDI; Range=1-313; Source=PubMed:10548058;.
MISCELLANEOUS: In the reverse direction L-lysine can act instead of L-ornithine, more slowly, yielding N(6)-(L-1-carboxyethyl)-L-lysine.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U23376; AAA86385.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A57499; A57499.

3D structure databases

ModBase

P15244.

Ontologies

GO:0047126;	Molecular function: N5-(carboxyethyl)ornithine synthase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007698; Ala_DHase/PNT_C.
IPR007886; Ala_DHase/PNT_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 313`	`313`	`N(5)-(carboxyethyl)ornithine synthase.`	`PRO_0000089483`
`NP_BIND`	`171 176`	`6`	`NADP (Potential).`
`MUTAGEN`	`15 15`		`R->K: Loss of activity.`

Sequence information

Length: 313 AA [This is the length of the unprocessed precursor]

Molecular weight: 35323 Da [This is the MW of the unprocessed precursor]

CRC64: B17FE0F477113C77 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIGLVKANF PGERRVPLLP KDIKDFKNEI LVEEGFGKFL DIDDQEYSDK GCHILSRAEV 

        70         80         90        100        110        120 
FAESEAIFSL KLIQPTDYYH LREGQMIIGW THPFGSGQSF MKEQALPKKL IVVDLDSNSP 

       130        140        150        160        170        180 
CIYYENEIFE SGIPKGLLYK NSFYAGYAGV LDALLQYGLI PTEETKIAIL GSGNVAQGAF 

       190        200        210        220        230        240 
SSISKYSSNI RMYYRKTMSI FKENYTKYDI IINGIEIGKD DDPILSFSEQ KSLKKGTLII 

       250        260        270        280        290        300 
DVAADAGNTI EGSHFTSIDA PIYENAGKYY YVVPNTPSLI YRNVSQELSK ILSENIFRKD 

       310 
CSRFIEKVKP LNK

P15244 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools